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OJBTM

 Online Journal of Bioinformatics © 

 Volume 13 (1):41-49, 2012.


Simulation of riboflavin synthase in Eremothecium gossypii  conversion of 6,7-dimethyl-8-ribityllumazine to riboflavin

 

Syarifuddin Idrus and Usman S.F. Tambunan

 

Department of Chemistry, Faculty of Mathematics and Science, University of Indonesia,  Depok 16424 Indonesia.


ABSTRACT

 

Idrus S, Tambunan USF., Simulation of riboflavin synthase in Eremothecium gossypii  converting 6,7-dimethyl-8-ribityllumazine  to  riboflavin, Online J Bioinform., 13 (1):41-49, 2012. Riboflavin synthase catalyzes conversion of two molecules of 6,7-dimethyl-8-ribityllumazine into one of riboflavin. An In silico simulation of riboflavin synthase of Eremothecium gossypii to convert 6,7-dimethyl-8-ribityllumazine to riboflavin is described.  Thermal stability of the enzyme was conducted using molecular dynamic simulation at 300K, 315K, 325K, 335K, and 350K. Substrate-interacted residues were Ser152, Thr154, Ser167, and Thr172 at the C-terminal domain and Glu22, Cys54, Thr56, Ala70, Thr73, and His108 at the N-terminal. Only one enzyme active site (N-terminal domain) catalyzed riboflavin formation. His108 was an active site from the N-terminal domain, which acted at an early stage of the riboflavin catalysis reaction.

                     

                      Key words: Simulation studies, Riboflavin synthase, Riboflavin, Eremothecium gossypii,     Molecular Dynamics.


 

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